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[1]
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NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=ATCC VR-613 / Malish 7;
DOI=10.1126/science.1061471; PubMed=11557893 [NCBI, ExPASy, EBI, Israel, Japan]
Ogata H.,
Audic S.,
Renesto-Audiffren P.,
Fournier P.-E.,
Barbe V.,
Samson D.,
Roux V.,
Cossart P.,
Weissenbach J.,
Claverie J.-M.,
Raoult D.;
"Mechanisms of evolution in Rickettsia conorii and R. prowazekii.";
Science 293:2093-2098(2001).
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- FUNCTION: The pyruvate dehydrogenase complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2). It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and lipoamide dehydrogenase (E3) (By similarity).
- CATALYTIC ACTIVITY: Pyruvate + [dihydrolipoyllysine-residue acetyltransferase] lipoyllysine = [dihydrolipoyllysine-residue acetyltransferase] S-acetyldihydrolipoyllysine + CO2.
- COFACTOR: Thiamine pyrophosphate (By similarity).
- SUBUNIT: Heterodimer of an alpha and a beta chain.
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Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms.
Distributed under the Creative Commons Attribution-NoDerivs License.
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| Length: 326 AA [This is the length of the unprocessed precursor] |
Molecular weight: 35821 Da [This is the MW of the unprocessed precursor] |
CRC64: 21A97CE0774EA9AE [This is a checksum on the sequence] |
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10 20 30 40 50 60
MQITVREALR DAMQEEMIRD DKVFVIGEEV AEYQGAYKVT QGLLEQFGPK RVIDTPITEY
70 80 90 100 110 120
GFAGLAVGAA FAGLRPIVEF MTFNFAMQAF DHIVNSAAKT HYMSGGQVKC PIVFRGPNGA
130 140 150 160 170 180
ASRVAAQHSQ NYTACYSHIP GLKVVAPYSA EDHKGLMLTA IRDDNPVVFL ENEILYGHSF
190 200 210 220 230 240
DVPKTIEPIP FGQAKILREG SSVTIVTFSI QVKLALDAAN FVQNDNIDCE VIDLRTIKPL
250 260 270 280 290 300
DTETIIESVK KTNRLVVVEE GWFFAGVGAS IASIVMKEAF DYLDAPIEIV SGKDLPLPYA
310 320
VNLETLALPS ESDVIEAVKK VCYYSI
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Q92IS2 in FASTA format |
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